Structure of PDB 5fgj Chain D

Receptor sequence
>5fgjD (length=422) Species: 10116 (Rattus norvegicus) [Search protein sequence]
TSYIEDNSNQNGAISLIFSLKEEVGALAKVLRLFEENDINLTHIESRPSR
LNKDEYEFFTYLDKRTKPVLGSIIKSLRNDIGATVHELSRDKEKNTVPWF
PRTIQELDRFANQILDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRV
EYTEEEKQTWGTVFRTLKALYKTHACYEHNHIFPLLEKYCGFREDNIPQL
EDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMY
TPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWF
TVEFGLCKEGDSIKAYGAGLLSSFGELQYCLSDKPKLLPLELEKTACQEY
SVTEFQPLYYVAESFSDAKEKVRTFAATIPRPFSVRYDPYTQRVEVLDNT
QQLKILADSINSEVGILCNALQ
3D structure
PDB5fgj Domain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering.
ChainD
Resolution3.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H285 H290 E330 S349
Catalytic site (residue number reindexed from 1) H258 H263 E303 S322
Enzyme Commision number 1.14.16.1: phenylalanine 4-monooxygenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FE D H285 H290 E330 H258 H263 E303
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0004505 phenylalanine 4-monooxygenase activity
GO:0005506 iron ion binding
GO:0016597 amino acid binding
GO:0016714 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006558 L-phenylalanine metabolic process
GO:0006559 L-phenylalanine catabolic process
GO:0006571 tyrosine biosynthetic process
GO:0009072 aromatic amino acid metabolic process
GO:0019293 tyrosine biosynthetic process, by oxidation of phenylalanine

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Molecular Function
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Biological Process
External links
PDB RCSB:5fgj, PDBe:5fgj, PDBj:5fgj
PDBsum5fgj
PubMed27145334
UniProtP04176|PH4H_RAT Phenylalanine-4-hydroxylase (Gene Name=Pah)

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